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Protein

Proteinase-activated receptor 1

Gene

F2r

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Blood coagulation, Hemostasis

Names & Taxonomyi

Protein namesi
Recommended name:
Proteinase-activated receptor 1
Short name:
PAR-1
Alternative name(s):
Thrombin receptor
Gene namesi
Name:F2r
Synonyms:Par1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2586. F2r.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini46 – 109ExtracellularSequence analysisAdd BLAST64
Transmembranei110 – 135Helical; Name=1Sequence analysisAdd BLAST26
Topological domaini136 – 144CytoplasmicSequence analysis9
Transmembranei145 – 164Helical; Name=2Sequence analysisAdd BLAST20
Topological domaini165 – 183ExtracellularSequence analysisAdd BLAST19
Transmembranei184 – 205Helical; Name=3Sequence analysisAdd BLAST22
Topological domaini206 – 225CytoplasmicSequence analysisAdd BLAST20
Transmembranei226 – 246Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini247 – 275ExtracellularSequence analysisAdd BLAST29
Transmembranei276 – 295Helical; Name=5Sequence analysisAdd BLAST20
Topological domaini296 – 318CytoplasmicSequence analysisAdd BLAST23
Transmembranei319 – 341Helical; Name=6Sequence analysisAdd BLAST23
Topological domaini342 – 357ExtracellularSequence analysisAdd BLAST16
Transmembranei358 – 381Helical; Name=7Sequence analysisAdd BLAST24
Topological domaini382 – 432CytoplasmicSequence analysisAdd BLAST51

GO - Cellular componenti

  • caveola Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
  • neuromuscular junction Source: RGD
  • plasma membrane Source: RGD
  • platelet dense tubular network Source: UniProtKB
  • postsynaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL6041.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21By similarityAdd BLAST21
PropeptideiPRO_000001274622 – 45Removed for receptor activationBy similarityAdd BLAST24
ChainiPRO_000001274746 – 432Proteinase-activated receptor 1Add BLAST387

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi69N-linked (GlcNAc...)Sequence analysis1
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi182 ↔ 261PROSITE-ProRule annotation
Glycosylationi257N-linked (GlcNAc...)Sequence analysis1
Glycosylationi266N-linked (GlcNAc...)Sequence analysis1
Modified residuei425PhosphoserineBy similarity1

Post-translational modificationi

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei45 – 46Cleavage; by thrombinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP26824.
PRIDEiP26824.

PTM databases

PhosphoSitePlusiP26824.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000065624.

Structurei

3D structure databases

ProteinModelPortaliP26824.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi64 – 68Asp/Glu-rich (acidic)5
Compositional biasi87 – 93Poly-Pro7

Domaini

The cleaved signal peptide may not be degraded and may function as an intracellular angiogenesis inhibitor peptide known as parstatin.By similarity

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJCV. Eukaryota.
ENOG4110Q89. LUCA.
HOGENOMiHOG000232200.
HOVERGENiHBG108233.
InParanoidiP26824.
PhylomeDBiP26824.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003912. Protea_act_rcpt.
IPR000935. Thrmbn_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR00908. THROMBINR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPRRLLLVA VGLSLCGPLL SSRVPMRQPE SERMYATPYA TPNPRSFFLR
60 70 80 90 100
NPSEDTFEQF PLGDEEEKNE SIPLEGRAVY LNKSRFPPMP PPPFISEDAS
110 120 130 140 150
GYLTSPWLTL FIPSVYTFVF IVSLPLNILA IAVFVFRMKV KKPAVVYMLH
160 170 180 190 200
LAMADVLFVS VLPFKISYYF SGTDWQFGSG MCRFATAACY CNMYASIMLM
210 220 230 240 250
TVISIDRFLA VVYPIQSLSW RTLGRANFTC VVIWVMAIMG VVPLLLKEQT
260 270 280 290 300
TQVPGLNITT CHDVLNETLL HGFYSYYFSA FSAIFFLVPL IISTVCYTSI
310 320 330 340 350
IRCLSSSAVA NRSKKSRALF LSAAVFCIFI VCFGPTNVLL IVHYLLLSDS
360 370 380 390 400
PGTETAYFAY LLCVCVTSVA SCIDPLIYYY ASSECQKHLY SILCCRESSD
410 420 430
SNSCNSTGQL MPSKMDTCSS HLNNSIYKKL LA
Length:432
Mass (Da):48,281
Last modified:August 1, 1992 - v1
Checksum:iDD032B97ABA4A605
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81642 mRNA. Translation: AAA42274.1.
PIRiA43448.
UniGeneiRn.2609.

Genome annotation databases

UCSCiRGD:2586. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81642 mRNA. Translation: AAA42274.1.
PIRiA43448.
UniGeneiRn.2609.

3D structure databases

ProteinModelPortaliP26824.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000065624.

Chemistry databases

ChEMBLiCHEMBL6041.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSitePlusiP26824.

Proteomic databases

PaxDbiP26824.
PRIDEiP26824.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2586. rat.

Organism-specific databases

RGDi2586. F2r.

Phylogenomic databases

eggNOGiENOG410IJCV. Eukaryota.
ENOG4110Q89. LUCA.
HOGENOMiHOG000232200.
HOVERGENiHBG108233.
InParanoidiP26824.
PhylomeDBiP26824.

Miscellaneous databases

PROiP26824.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003912. Protea_act_rcpt.
IPR000935. Thrmbn_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR00908. THROMBINR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAR1_RAT
AccessioniPrimary (citable) accession number: P26824
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.